Evidence map›Paper›PMID 34282309›Full record

ArticleNature microbiology2021

MX2-mediated innate immunity against HIV-1 is regulated by serine phosphorylation.

Gilberto Betancor, Jose M Jimenez-Guardeño, Steven Lynham, Robin Antrobus, Hataf Khan, Andrew Sobala, Matthew D J Dicks, Michael H Malim

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. MX2 Mediates Collapse of the HIV-1 Capsid.bioRxiv : the preprint server for biology · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Gilberto BetancorDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK. gilberto.betancor@kcl.ac.uk.ORCID http://orcid.org/0000-0003-0548-7690
Jose M Jimenez-GuardeñoDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK.ORCID http://orcid.org/0000-0002-1726-8033
Steven LynhamCentre of Excellence for Mass Spectrometry, The James Black Centre, King's College London, London, UK.
Robin AntrobusCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, UK.
Hataf KhanDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK.
Andrew SobalaDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK.
Matthew D J DicksDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK.
Michael H MalimDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK. michael.malim@kcl.ac.uk.ORCID http://orcid.org/0000-0002-7699-2064
King's College London · GBUniversity of Cambridge · GB

Funding

X-ray Crystallographic Fragment Screening CoreU54AI150472 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI LYUMKIS, DMITRY · 2019 to 2021
$15.7M
X-ray Crystallographic Fragment Screening CoreU54GM103368 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SARAFIANOS, STEFAN G, TORBETT, BRUCE EDWARD · 2017 to 2018
$11.1M
Medical Research Council MR/M001199/1NIAID NIH HHS U54 AI150472NIGMS NIH HHS U54 GM103368Wellcome Trust 106223Wellcome Trust 106223/Z/14/Z
6 · The paper itself

Abstract

The antiviral cytokine interferon activates expression of interferon-stimulated genes to establish an antiviral state. Myxovirus resistance 2 (MX2, also known as MxB) is an interferon-stimulated gene that inhibits the nuclear import of HIV-1 and interacts with the viral capsid and cellular nuclear transport machinery. Here, we identified the myosin light chain phosphatase (MLCP) subunits myosin phosphatase target subunit 1 (MYPT1) and protein phosphatase 1 catalytic subunit-β (PPP1CB) as positively-acting regulators of MX2, interacting with its amino-terminal domain. We demonstrated that serine phosphorylation of the N-terminal domain at positions 14, 17 and 18 suppresses MX2 antiviral function, prevents interactions with the HIV-1 capsid and nuclear transport factors, and is reversed by MLCP. Notably, serine phosphorylation of the N-terminal domain also impedes MX2-mediated inhibition of nuclear import of cellular karyophilic cargo. We also found that interferon treatment reduces levels of phosphorylation at these serine residues and outline a homeostatic regulatory mechanism in which repression of MX2 by phosphorylation, together with MLCP-mediated dephosphorylation, balances the deleterious effects of MX2 on normal cell function with innate immunity against HIV-1.

Indexed as

Immunity, InnateAmino Acid MotifsHeLa CellsHIV-1HIV InfectionsHumansMyosin-Light-Chain PhosphataseMyxovirus Resistance ProteinsPhosphorylationProtein DomainsProtein Phosphatase 1SerineMX2 protein, humanMyosin-Light-Chain PhosphataseMyxovirus Resistance ProteinsPPP1CB protein, humanPPP1R12A protein, humanProtein Phosphatase 1Serine

Identifiers

PMID34282309
PMCPMC7611661
OpenAlexW3186282898

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.